AT221_ASPFU
ID AT221_ASPFU Reviewed; 609 AA.
AC Q4WH97;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; ORFNames=AFUA_2G06170;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Vacuolar effluxer which mediate the efflux of amino acids
CC resulting from autophagic degradation. The release of autophagic amino
CC acids allows the maintenance of protein synthesis and viability during
CC nitrogen starvation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Vacuole and punctate structures.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG22 family. {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87708.1; -; Genomic_DNA.
DR RefSeq; XP_749746.1; XM_744653.1.
DR AlphaFoldDB; Q4WH97; -.
DR STRING; 746128.CADAFUBP00002268; -.
DR EnsemblFungi; EAL87708; EAL87708; AFUA_2G06170.
DR GeneID; 3506649; -.
DR KEGG; afm:AFUA_2G06170; -.
DR VEuPathDB; FungiDB:Afu2g06170; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR InParanoid; Q4WH97; -.
DR OMA; MYPLGAV; -.
DR OrthoDB; 1460747at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd17483; MFS_Atg22_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR044738; Atg22.
DR InterPro; IPR024671; Atg22-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF11700; ATG22; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..609
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000207617"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 214..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 66275 MW; 609A5860ACBEE91C CRC64;
MRAGHETETS IMRPQYPGDD IRPTSKKELA GWYSYGWAAE VFTVCAMGSF LPITLEQMAR
DRGVLFSDKV TPCSATLNGP SRMSIQARWT LSSRYDAGRP TVANQCVVYI FGVEINTASF
AMYTFSVSVF IQAILIISMS GAADHGSHRK LLLMAFAVIG SVSTMLFLGV VPKIYMVGAV
IAIIANTCFG ASFVLLNSFL PLLVRHHPSV LRSAREPRPA LDDSRAQEGH SDTTNGIEHG
IESNVTSPLL HARQGNGENA EADMHPATHI TVSQELKVST RISSFGIGIG YIGAIILQIV
CILVVIATNQ TTYSLRLVLF LIGLWWFIFS IPAALWLRSR PGPPLATTHH GKHTRSWIGY
MAYSWKSLYR TAVRTRHLKD ILLFLAAWLL LSDGIATVSG TAVLFAKTQL NMQPAALGLI
NVIAMVAGVL GAFSWGSFSR VFNLSASQTI IACILLFELV PLYGLLGFIP AIKSLGFLGL
QQPWEMFPLG IVYGLVMGGL SSYCRSFFGE LIPPGNEAAF YALYAITDKG SSIFGPTIVG
IITDRYGEIR PAFVFLAILI FLPLPLMLLV DVERGKRDAL ALAAELQPSG AQTYGTLPTN
EDRAPPSEL
